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3KRS

Structure of Triosephosphate Isomerase from Cryptosporidium Parvum at 1.55A Resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0019563biological_processglycerol catabolic process
A0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
B0004807molecular_functiontriose-phosphate isomerase activity
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0019563biological_processglycerol catabolic process
B0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 301
ChainResidue
ATYR5
AILE223
ACYS225
AILE228
AHOH322
AHOH362

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 301
ChainResidue
BILE228
BHOH321
BHOH974
BTYR5
BILE223
BCYS225

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPIWAIGTG
ChainResidueDetails
AALA165-GLY175

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
AHIS97
AASN10
AGLU167
AGLY173
ALYS12

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
BHIS97
BASN10
BGLU167
BGLY173
BLYS12

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PDB entries from 2024-07-17

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